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6I8Z

Crystal structure of PTK2 in complex with BI-4464.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue H82 A 701
ChainResidue
AILE428
AGLU506
AARG550
ALEU553
AGLY563
AASP564
ALEU567
AHOH913
AGLN438
AALA452
AMET499
AGLU500
ALEU501
ACYS502
ATHR503
AGLY505

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues27
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGQFGDVHqGiymspenpala.......VAIK
ChainResidueDetails
AILE428-LYS454

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDIAARNVLV
ChainResidueDetails
APHE542-VAL554

site_idPS00661
Number of Residues31
DetailsFERM_2 FERM domain signature 2. HrdiaarnvlVSsndCVklgDfgLsrYMeDS
ChainResidueDetails
AHIS544-SER574

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12467573","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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